|
Name |
Accession |
Description |
Interval |
E-value |
| DnaJ-X |
pfam14308 |
X-domain of DnaJ-containing; IN certain plant and yeast proteins, the DnaJ-1 proteins have a ... |
316-516 |
1.74e-47 |
|
X-domain of DnaJ-containing; IN certain plant and yeast proteins, the DnaJ-1 proteins have a three-domain structure. The x-domain lies between the N-terminal DnaJ and the C-terminal Z domains. The exact function is not known.
Pssm-ID: 433858 Cd Length: 205 Bit Score: 163.86 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 316 QNKREVQLALHLRDMINNYIFGDP-----DDYIIKFSQQIKELCQTSFGHIILENVAWSYENCANQFLGEKySLFGISGK 390
Cdd:pfam14308 1 QKEREEELAEKLRDRLSPYVEADKpgdvlDEFEEKLEEEAEDLKLESFGVEILHTIGWVYENKAKSFLKSQ-KFLGVGGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 391 YYKMQQKKRVIGTGFKFVKTLIKTSSLANQIRKKEDDDDiSYEKTAKVNKKIEDSLPTIVETMLNICLIDIDQTIKGVCK 470
Cdd:pfam14308 80 FSSVKEKGRTVKNTWNTLSSALDAQSTMEEMAKEEEKGG-EELTEEELAKLEELLTGKILAAAWAGSKFEIESTLREVCD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1371546194 471 KVFTDMGVDENMRKTRAETLIILAKIMKKIIYDFKKNTEIMDTKKL 516
Cdd:pfam14308 159 KVLKDKSVPKKTRIKRAEALLILGKIFQKAKRDPEEEEEARVFEEL 204
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
189-516 |
4.61e-33 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 134.53 E-value: 4.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 189 IKVKNDEFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQF 268
Cdd:PTZ00341 568 IEIPDTLFYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKFGYDGIKGVNF 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 269 IDSTFFFtLLFGSEKLDPYIGKLRMVMYVEY---EQLY------KDEDVQRLIIKEQNKREVQLALHLRDMINNYIFGDp 339
Cdd:PTZ00341 648 IHPSIFY-LLASLEKFADFTGSPQIVTLLKFffeKKLSmndldnKSEHLLKFMEQYQKEREAHISENLINILQPCIAGD- 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 340 DDYIIKFSQQIKELCQTSFGHIILENVAWSYENCANQFLGEKyslfgiSGKYYKMQQ-----KKRVIGTGFKFVKTL--- 411
Cdd:PTZ00341 726 RKWDVPIIDKIEELKGSPFDIAIIDSIGWIFKHVAKSHLKKP------KKAAKKLEQrskanKEELANENNKLMNILkey 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 412 IKTSSLANQIR------KKEDDDDISYEKTAKVN-KKIEDSLPTIVETMLNICLIDIDQTIKGVCKKVFTDMGVDENMRK 484
Cdd:PTZ00341 800 FGNNEQINSITynfeniNLNEDNENGSKKILDLNhKDQKEIFEEIISYIVDISLSDIENTAKNAAEQILSDEGLDEKKLK 879
|
330 340 350
....*....|....*....|....*....|....
gi 1371546194 485 TRAETLIILAKIMKKIIYDFKKNTEI--MDTKKL 516
Cdd:PTZ00341 880 KRAESLKKLANAIEKYAGGGKKDKKAkkKDAKDL 913
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
196-267 |
4.54e-24 |
|
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 97.85 E-value: 4.54e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546194 196 FYRILKVPTDASQNEIKRQYYKLAKEFHPDKC-SDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQ 267
Cdd:COG0484 2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNpGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLA 74
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
195-256 |
2.64e-23 |
|
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.
Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 92.92 E-value: 2.64e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLK-AKEQFQKIGEAYQVLGDVERRRRYD 256
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPeAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
196-312 |
7.35e-21 |
|
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.
Pssm-ID: 274090 [Multi-domain] Cd Length: 354 Bit Score: 94.20 E-value: 7.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 196 FYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAIN--------NMQ 267
Cdd:TIGR02349 2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNggggggggGFN 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546194 268 FIDSTFF------FTLLFG-------SEKLDPYIGK-LRMVMYVEYEQLY----KDEDVQRLI 312
Cdd:TIGR02349 82 GFDIGFFgdfgdiFGDFFGggggsgrRRRSGPRRGEdLRYDLELTFEEAVfgveKEIEIPRKE 144
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
195-310 |
5.52e-20 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 91.83 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNmQFIDSTFF 274
Cdd:PRK14298 6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDN-QYSAEDIF 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1371546194 275 -----------FTLLFG----SEKLDPYIGK-LRMVMYVEYEQ----LYKDEDVQR 310
Cdd:PRK14298 85 rgadfggfgdiFEMFFGgggrRGRMGPRRGSdLRYDLYITLEEaafgVRKDIDVPR 140
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
195-248 |
3.16e-19 |
|
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.
Pssm-ID: 99751 [Multi-domain] Cd Length: 55 Bit Score: 81.05 E-value: 3.16e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSD-LKAKEQFQKIGEAYQVLGD 248
Cdd:cd06257 1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
195-251 |
3.44e-18 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 78.43 E-value: 3.44e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLK--AKEQFQKIGEAYQVLGDVER 251
Cdd:smart00271 2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKeeAEEKFKEINEAYEVLSDPEK 60
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
195-340 |
5.50e-15 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 77.17 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINN---MQF--- 268
Cdd:NF037946 6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGeggFGFdaf 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546194 269 -IDSTFFFTLLFGSEKLDPYIGklrmvmyveyEQLYKDEDVQRLIIKEQNKREVQLALHLRDMINNYIfGDPD 340
Cdd:NF037946 86 dVFSSFFETINKSGAFLDDSVD----------ESVSADDDLDRLFDDSKEPSFTSGLDEIVQFWEAFI-GNPD 147
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
124-510 |
5.71e-03 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 39.59 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 124 NTPESITQKALGKIWDDEKreWYDFYYNLDEEANELLNITDDNKNNKYDRKKDTNNDEYYNKNGNIKVKNDEFYRILKVP 203
Cdd:COG3292 448 NTIYSILEDDNGNLWNFNS--ASNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLTLLLLA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 204 TDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQFIDSTFFFTLLFGSEK 283
Cdd:COG3292 526 LLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 284 LDPYIGKLRMVMYvEYEQLYKDEDVQRLIIKEQNKREVQLALHLRDMINNYIFGDPDDYIIKFSQQIKELCQTSFGHIIL 363
Cdd:COG3292 606 LILLLLLLLLLLL-LILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLL 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 364 ENVAWSYENCANQFLGEKYSLFGISGKYYKMQQKKRVIGTGFKFVKTLIKTSSLANQIRKKEDDDDISYEKTAKVNKKIE 443
Cdd:COG3292 685 LLLLLLALLLLLLLLLALKLLLLLLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLL 764
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371546194 444 DSLPTIVETMLNICLIDIDQTIKGVCKKVFTDMGVDENMRKTRAETLIILAKIMKKIIYDFKKNTEI 510
Cdd:COG3292 765 ILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKI 831
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DnaJ-X |
pfam14308 |
X-domain of DnaJ-containing; IN certain plant and yeast proteins, the DnaJ-1 proteins have a ... |
316-516 |
1.74e-47 |
|
X-domain of DnaJ-containing; IN certain plant and yeast proteins, the DnaJ-1 proteins have a three-domain structure. The x-domain lies between the N-terminal DnaJ and the C-terminal Z domains. The exact function is not known.
Pssm-ID: 433858 Cd Length: 205 Bit Score: 163.86 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 316 QNKREVQLALHLRDMINNYIFGDP-----DDYIIKFSQQIKELCQTSFGHIILENVAWSYENCANQFLGEKySLFGISGK 390
Cdd:pfam14308 1 QKEREEELAEKLRDRLSPYVEADKpgdvlDEFEEKLEEEAEDLKLESFGVEILHTIGWVYENKAKSFLKSQ-KFLGVGGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 391 YYKMQQKKRVIGTGFKFVKTLIKTSSLANQIRKKEDDDDiSYEKTAKVNKKIEDSLPTIVETMLNICLIDIDQTIKGVCK 470
Cdd:pfam14308 80 FSSVKEKGRTVKNTWNTLSSALDAQSTMEEMAKEEEKGG-EELTEEELAKLEELLTGKILAAAWAGSKFEIESTLREVCD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1371546194 471 KVFTDMGVDENMRKTRAETLIILAKIMKKIIYDFKKNTEIMDTKKL 516
Cdd:pfam14308 159 KVLKDKSVPKKTRIKRAEALLILGKIFQKAKRDPEEEEEARVFEEL 204
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
189-516 |
4.61e-33 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 134.53 E-value: 4.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 189 IKVKNDEFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQF 268
Cdd:PTZ00341 568 IEIPDTLFYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKFGYDGIKGVNF 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 269 IDSTFFFtLLFGSEKLDPYIGKLRMVMYVEY---EQLY------KDEDVQRLIIKEQNKREVQLALHLRDMINNYIFGDp 339
Cdd:PTZ00341 648 IHPSIFY-LLASLEKFADFTGSPQIVTLLKFffeKKLSmndldnKSEHLLKFMEQYQKEREAHISENLINILQPCIAGD- 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 340 DDYIIKFSQQIKELCQTSFGHIILENVAWSYENCANQFLGEKyslfgiSGKYYKMQQ-----KKRVIGTGFKFVKTL--- 411
Cdd:PTZ00341 726 RKWDVPIIDKIEELKGSPFDIAIIDSIGWIFKHVAKSHLKKP------KKAAKKLEQrskanKEELANENNKLMNILkey 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 412 IKTSSLANQIR------KKEDDDDISYEKTAKVN-KKIEDSLPTIVETMLNICLIDIDQTIKGVCKKVFTDMGVDENMRK 484
Cdd:PTZ00341 800 FGNNEQINSITynfeniNLNEDNENGSKKILDLNhKDQKEIFEEIISYIVDISLSDIENTAKNAAEQILSDEGLDEKKLK 879
|
330 340 350
....*....|....*....|....*....|....
gi 1371546194 485 TRAETLIILAKIMKKIIYDFKKNTEI--MDTKKL 516
Cdd:PTZ00341 880 KRAESLKKLANAIEKYAGGGKKDKKAkkKDAKDL 913
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
196-267 |
4.54e-24 |
|
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 97.85 E-value: 4.54e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546194 196 FYRILKVPTDASQNEIKRQYYKLAKEFHPDKC-SDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQ 267
Cdd:COG0484 2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNpGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLA 74
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
195-256 |
2.64e-23 |
|
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.
Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 92.92 E-value: 2.64e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLK-AKEQFQKIGEAYQVLGDVERRRRYD 256
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPeAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
196-312 |
7.35e-21 |
|
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.
Pssm-ID: 274090 [Multi-domain] Cd Length: 354 Bit Score: 94.20 E-value: 7.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 196 FYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAIN--------NMQ 267
Cdd:TIGR02349 2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNggggggggGFN 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546194 268 FIDSTFF------FTLLFG-------SEKLDPYIGK-LRMVMYVEYEQLY----KDEDVQRLI 312
Cdd:TIGR02349 82 GFDIGFFgdfgdiFGDFFGggggsgrRRRSGPRRGEdLRYDLELTFEEAVfgveKEIEIPRKE 144
|
|
| CbpA |
COG2214 |
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
194-262 |
5.05e-20 |
|
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 84.77 E-value: 5.05e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371546194 194 DEFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLK--AKEQFQKIGEAYQVLGDVERRRRYDKEGKNA 262
Cdd:COG2214 5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalAEELFQRLNEAYEVLSDPERRAEYDRELGQS 75
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
195-310 |
5.52e-20 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 91.83 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNmQFIDSTFF 274
Cdd:PRK14298 6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDN-QYSAEDIF 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1371546194 275 -----------FTLLFG----SEKLDPYIGK-LRMVMYVEYEQ----LYKDEDVQR 310
Cdd:PRK14298 85 rgadfggfgdiFEMFFGgggrRGRMGPRRGSdLRYDLYITLEEaafgVRKDIDVPR 140
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
195-248 |
3.16e-19 |
|
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.
Pssm-ID: 99751 [Multi-domain] Cd Length: 55 Bit Score: 81.05 E-value: 3.16e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSD-LKAKEQFQKIGEAYQVLGD 248
Cdd:cd06257 1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
195-251 |
3.44e-18 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 78.43 E-value: 3.44e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLK--AKEQFQKIGEAYQVLGDVER 251
Cdd:smart00271 2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKeeAEEKFKEINEAYEVLSDPEK 60
|
|
| PRK14299 |
PRK14299 |
chaperone protein DnaJ; Provisional |
195-262 |
6.88e-18 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 84.22 E-value: 6.88e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNA 262
Cdd:PRK14299 5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTA 72
|
|
| PRK14291 |
PRK14291 |
chaperone protein DnaJ; Provisional |
195-262 |
8.87e-18 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 85.21 E-value: 8.87e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNA 262
Cdd:PRK14291 4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAA 71
|
|
| PRK14295 |
PRK14295 |
molecular chaperone DnaJ; |
193-256 |
1.57e-17 |
|
molecular chaperone DnaJ;
Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 84.52 E-value: 1.57e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371546194 193 NDEFYRILKVPTDASQNEIKRQYYKLAKEFHPD-KCSDLKAKEQFQKIGEAYQVLGDVERRRRYD 256
Cdd:PRK14295 8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDaNKGDAKAEERFKEISEAYDVLSDEKKRKEYD 72
|
|
| PRK14276 |
PRK14276 |
chaperone protein DnaJ; Provisional |
193-264 |
2.19e-16 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 80.90 E-value: 2.19e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371546194 193 NDEFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAIN 264
Cdd:PRK14276 3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGAN 74
|
|
| PRK14277 |
PRK14277 |
chaperone protein DnaJ; Provisional |
195-281 |
2.57e-16 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 80.62 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPD-KCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQFIDSTF 273
Cdd:PRK14277 6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDlNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFDPGGFGQGGF 85
|
90
....*....|....*.
gi 1371546194 274 --------FFTLLFGS 281
Cdd:PRK14277 86 gqggfgggGFDFDFGG 101
|
|
| PRK10767 |
PRK10767 |
chaperone protein DnaJ; Provisional |
192-265 |
2.58e-16 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 80.57 E-value: 2.58e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371546194 192 KNDeFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLK-AKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINN 265
Cdd:PRK10767 3 KRD-YYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKeAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQ 76
|
|
| PRK14278 |
PRK14278 |
chaperone protein DnaJ; Provisional |
195-259 |
7.08e-16 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 79.33 E-value: 7.08e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEG 259
Cdd:PRK14278 4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVDLGG 68
|
|
| PRK14293 |
PRK14293 |
molecular chaperone DnaJ; |
195-259 |
9.24e-16 |
|
molecular chaperone DnaJ;
Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 78.88 E-value: 9.24e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEG 259
Cdd:PRK14293 4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQFG 68
|
|
| PRK14301 |
PRK14301 |
chaperone protein DnaJ; Provisional |
195-265 |
1.15e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 78.63 E-value: 1.15e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSD-LKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINN 265
Cdd:PRK14301 5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDnPEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVNG 76
|
|
| PTZ00037 |
PTZ00037 |
DnaJ_C chaperone protein; Provisional |
191-283 |
2.56e-15 |
|
DnaJ_C chaperone protein; Provisional
Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 77.94 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 191 VKNDEFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDlkaKEQFQKIGEAYQVLGDVERRRRYDKEGKNAI-NNMQFI 269
Cdd:PTZ00037 25 VDNEKLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD---PEKFKEISRAYEVLSDPEKRKIYDEYGEEGLeGGEQPA 101
|
90
....*....|....
gi 1371546194 270 DSTFFFTLLFGSEK 283
Cdd:PTZ00037 102 DASDLFDLIFGGGR 115
|
|
| PRK14279 |
PRK14279 |
molecular chaperone DnaJ; |
193-256 |
4.46e-15 |
|
molecular chaperone DnaJ;
Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 77.08 E-value: 4.46e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371546194 193 NDEFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCS-DLKAKEQFQKIGEAYQVLGDVERRRRYD 256
Cdd:PRK14279 8 EKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPgDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
|
|
| PRK14294 |
PRK14294 |
chaperone protein DnaJ; Provisional |
191-274 |
4.83e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 76.73 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 191 VKNDeFYRILKVPTDASQNEIKRQYYKLAKEFHPDKC-SDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQFI 269
Cdd:PRK14294 2 VKRD-YYEILGVTRDASEEEIKKSYRKLAMKYHPDRNpGDKEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGTGFS 80
|
....*
gi 1371546194 270 DSTFF 274
Cdd:PRK14294 81 GFSGF 85
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
195-340 |
5.50e-15 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 77.17 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINN---MQF--- 268
Cdd:NF037946 6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGeggFGFdaf 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546194 269 -IDSTFFFTLLFGSEKLDPYIGklrmvmyveyEQLYKDEDVQRLIIKEQNKREVQLALHLRDMINNYIfGDPD 340
Cdd:NF037946 86 dVFSSFFETINKSGAFLDDSVD----------ESVSADDDLDRLFDDSKEPSFTSGLDEIVQFWEAFI-GNPD 147
|
|
| PRK14282 |
PRK14282 |
chaperone protein DnaJ; Provisional |
190-259 |
5.71e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 76.37 E-value: 5.71e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371546194 190 KVKNDeFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLK--AKEQFQKIGEAYQVLGDVERRRRYDKEG 259
Cdd:PRK14282 1 REKKD-YYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRkeAEQKFKEIQEAYEVLSDPQKRAMYDRFG 71
|
|
| PRK14281 |
PRK14281 |
chaperone protein DnaJ; Provisional |
195-259 |
1.05e-14 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 76.00 E-value: 1.05e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLK-AKEQFQKIGEAYQVLGDVERRRRYDKEG 259
Cdd:PRK14281 4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKeAEEHFKEVNEAYEVLSNDDKRRRYDQFG 69
|
|
| PRK14283 |
PRK14283 |
chaperone protein DnaJ; Provisional |
195-281 |
2.16e-14 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 74.86 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEG---------KNAINN 265
Cdd:PRK14283 6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQFGhagmdgfsqEDIFNN 85
|
90
....*....|....*.
gi 1371546194 266 MQFIDSTFFFTLLFGS 281
Cdd:PRK14283 86 INFEDIFQGFGFGIGN 101
|
|
| PRK14280 |
PRK14280 |
molecular chaperone DnaJ; |
195-259 |
2.41e-14 |
|
molecular chaperone DnaJ;
Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 74.76 E-value: 2.41e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEG 259
Cdd:PRK14280 5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQFG 69
|
|
| PRK14300 |
PRK14300 |
chaperone protein DnaJ; Provisional |
195-267 |
9.67e-14 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 72.74 E-value: 9.67e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQ 267
Cdd:PRK14300 4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQNQQ 76
|
|
| PRK14292 |
PRK14292 |
chaperone protein DnaJ; Provisional |
195-259 |
1.20e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 72.61 E-value: 1.20e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEG 259
Cdd:PRK14292 3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDRFG 67
|
|
| PRK14284 |
PRK14284 |
chaperone protein DnaJ; Provisional |
195-262 |
1.65e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 72.18 E-value: 1.65e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCS-DLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNA 262
Cdd:PRK14284 2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPgDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKDG 70
|
|
| PRK14297 |
PRK14297 |
molecular chaperone DnaJ; |
193-264 |
3.96e-13 |
|
molecular chaperone DnaJ;
Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 70.97 E-value: 3.96e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546194 193 NDEFYRILKVPTDASQNEIKRQYYKLAKEFHPDK-CSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAIN 264
Cdd:PRK14297 3 SKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKnKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFN 75
|
|
| PRK14289 |
PRK14289 |
molecular chaperone DnaJ; |
195-265 |
8.65e-13 |
|
molecular chaperone DnaJ;
Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 69.86 E-value: 8.65e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKC-SDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINN 265
Cdd:PRK14289 6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNpGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVGG 77
|
|
| PRK14290 |
PRK14290 |
chaperone protein DnaJ; Provisional |
195-259 |
9.01e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 69.57 E-value: 9.01e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLK--AKEQFQKIGEAYQVLGDVERRRRYDKEG 259
Cdd:PRK14290 4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKaeAEEKFKEISEAYEVLSDPQKRRQYDQTG 70
|
|
| PRK14286 |
PRK14286 |
chaperone protein DnaJ; Provisional |
196-264 |
2.59e-12 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 68.48 E-value: 2.59e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 196 FYRILKVPTDASQNEIKRQYYKLAKEFHPDKCS-DLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAIN 264
Cdd:PRK14286 6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKgNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVN 75
|
|
| PRK10266 |
PRK10266 |
curved DNA-binding protein; |
195-257 |
3.22e-11 |
|
curved DNA-binding protein;
Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 64.46 E-value: 3.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371546194 195 EFYRILKV-PTDaSQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDK 257
Cdd:PRK10266 5 DYYAIMGVkPTD-DLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQ 67
|
|
| PRK14288 |
PRK14288 |
molecular chaperone DnaJ; |
196-273 |
8.43e-11 |
|
molecular chaperone DnaJ;
Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 63.55 E-value: 8.43e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371546194 196 FYRILKVPTDASQNEIKRQYYKLAKEFHPDK-CSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQFIDSTF 273
Cdd:PRK14288 5 YYEILEVEKHSNQETIKKSYRKLALKYHPDRnAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGASQSDF 83
|
|
| DjlA |
COG1076 |
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
194-246 |
8.91e-11 |
|
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 57.88 E-value: 8.91e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 194 DEFYRILKVPTDASQNEIKRQYYKLAKEFHPDK----CSD---LKAKEQFQKIGEAYQVL 246
Cdd:COG1076 4 DDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaagLPEeeqRLALQKAAAINEAYETL 63
|
|
| PRK14287 |
PRK14287 |
chaperone protein DnaJ; Provisional |
195-259 |
1.82e-10 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 62.72 E-value: 1.82e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEG 259
Cdd:PRK14287 5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFG 69
|
|
| PRK14296 |
PRK14296 |
chaperone protein DnaJ; Provisional |
191-273 |
1.98e-10 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 62.66 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 191 VKNDEFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQFID 270
Cdd:PRK14296 1 MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHAAFDGSSGFS 80
|
...
gi 1371546194 271 STF 273
Cdd:PRK14296 81 SNF 83
|
|
| PRK14285 |
PRK14285 |
chaperone protein DnaJ; Provisional |
195-262 |
4.28e-09 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 58.46 E-value: 4.28e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371546194 195 EFYRILKVPTDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQ-FQKIGEAYQVLGDVERRRRYDKEGKNA 262
Cdd:PRK14285 4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESiFKEATEAYEVLIDDNKRAQYDRFGHTA 72
|
|
| PTZ00475 |
PTZ00475 |
RESA-like protein; Provisional |
266-497 |
1.84e-07 |
|
RESA-like protein; Provisional
Pssm-ID: 185654 Cd Length: 282 Bit Score: 52.72 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 266 MQFIDSTFFFTLLFGSEKLDPYIGKLRMVMYVEY---------EQLYKDEDVQRLIIKEQNKREVQLALHLRDMINNYIf 336
Cdd:PTZ00475 1 MIIIVPFIFFNLIFTSDMMYEYIENTKVPIFVKLffgksifieDIFYYVGMIMKEMMEGQNIREEEVAELLKDRLDLYI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 337 GDPDDYIIKFSQQIKELCQTSFGHIILENVAWSYENCANQFLGEKYSlFGISGK-YYKMQQKKRVIGTG----------- 404
Cdd:PTZ00475 80 DNEDEWEKLMENEISMLLKSSFSNFILESIGWTYENVSNIFLEEKAN-SGINKKdIYLKEANERMIRNSivlrqcksrfi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 405 --------FK-----FVKTLIKTSS-------LANQIRKKEDD-----DDISYEKTAK-VNKKIEDSLPTIVETMLNICL 458
Cdd:PTZ00475 159 siitnyypFKeqnnpFIKQAQYVSSsnyvlddIINNIDYSIDNihraiDNLYYEHILNlLEEEKNEILEEILRNILKIIL 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 1371546194 459 IDIDQTIKGVCKKVFTDMGVDENMRKTRAETLIILAKIM 497
Cdd:PTZ00475 239 CDVETTVRRSAQKVLQNAEGDTNLMLKRAKGLQSLGKMI 277
|
|
| djlA |
PRK09430 |
co-chaperone DjlA; |
197-243 |
3.95e-05 |
|
co-chaperone DjlA;
Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 45.57 E-value: 3.95e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1371546194 197 YRILKVPTDASQNEIKRQYYKLAKEFHPDKcsdL--K---------AKEQFQKIGEAY 243
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDK---LvaKglppemmemAKEKAQEIQAAY 257
|
|
| hscB |
PRK00294 |
co-chaperone HscB; Provisional |
208-255 |
1.87e-03 |
|
co-chaperone HscB; Provisional
Pssm-ID: 166894 [Multi-domain] Cd Length: 173 Bit Score: 39.45 E-value: 1.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1371546194 208 QNEIKRQYYKLAKEFHPDKCSDLKAKEQFQ------KIGEAYQVLGDVERRRRY 255
Cdd:PRK00294 20 LDQLATRYRELAREVHPDRFADAPEREQRLalersaSLNEAYQTLKSPPRRARY 73
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
124-510 |
5.71e-03 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 39.59 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 124 NTPESITQKALGKIWDDEKreWYDFYYNLDEEANELLNITDDNKNNKYDRKKDTNNDEYYNKNGNIKVKNDEFYRILKVP 203
Cdd:COG3292 448 NTIYSILEDDNGNLWNFNS--ASNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLTLLLLA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 204 TDASQNEIKRQYYKLAKEFHPDKCSDLKAKEQFQKIGEAYQVLGDVERRRRYDKEGKNAINNMQFIDSTFFFTLLFGSEK 283
Cdd:COG3292 526 LLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLILLLLLLRLLLLLLLLELLERLLALLLEIELLLTLLLLLLLLLLLLLLL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 284 LDPYIGKLRMVMYvEYEQLYKDEDVQRLIIKEQNKREVQLALHLRDMINNYIFGDPDDYIIKFSQQIKELCQTSFGHIIL 363
Cdd:COG3292 606 LILLLLLLLLLLL-LILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLELELLLELLLLLAELILELLLILLLL 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546194 364 ENVAWSYENCANQFLGEKYSLFGISGKYYKMQQKKRVIGTGFKFVKTLIKTSSLANQIRKKEDDDDISYEKTAKVNKKIE 443
Cdd:COG3292 685 LLLLLLALLLLLLLLLALKLLLLLLLILLLLLLLLGLLLLLLDLVLLLLLLILLIILLLLILLEELLLANDIELEGILLL 764
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371546194 444 DSLPTIVETMLNICLIDIDQTIKGVCKKVFTDMGVDENMRKTRAETLIILAKIMKKIIYDFKKNTEI 510
Cdd:COG3292 765 ILLVLELLLELALGLILLLKLLLLLLNLLIGLIKETVSEGSILLKLLVLELELAESVLIALEGLGKI 831
|
|
| |
